skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Intracellular localization of varicella-zoster virus ORF39 protein and its functional relationship to glycoprotein K

Abstract

Varicella-zoster virus (VZV) encodes two multiply inserted membrane proteins, open reading frame (ORF) 39 protein (ORF39p) and glycoprotein K (gK). The HSV-1 homologs of these proteins are believed to act in conjunction with each other during viral egress and cell-cell fusion, and they directly influence each other's intracellular trafficking. However, ORF39p and VZV gK have received very limited study largely due to difficulties in producing antibodies to these highly hydrophobic proteins. To overcome this obstacle, we introduced epitope tags into both ORF39p and gK and examined their intracellular distributions in transfected and infected cells. Our data demonstrate that both ORF39p and gK accumulate predominately in the ER of cultured cells when expressed in the absence of other VZV proteins or when coexpressed in isolation from other VZV proteins. Therefore, the transport of VZV ORF39p and gK does not exhibit the functional interdependence seen in their HSV-1 homologs. However, during infection, the primary distributions of ORF39p and gK shift from the ER to the Golgi, and they are also found in the plasma membrane indicating that their intracellular trafficking during infection depends on other VZV-encoded proteins. During infection, ORF39p and gK tightly colocalize with VZV envelope glycoproteins B, E and H;more » however, the coexpression of ORF39p or gK with other individual viral glycoproteins is insufficient to alter the transport of either ORF39p or gK.« less

Authors:
 [1];  [1];  [2]
  1. Division of Infectious Diseases and Immunology, Saint Louis University School of Medicine, St. Louis, MO 63110-0250 (United States)
  2. Division of Infectious Diseases and Immunology, Saint Louis University School of Medicine, St. Louis, MO 63110-0250 (United States). E-mail: heinemtc@slu.edu
Publication Date:
OSTI Identifier:
20975214
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 358; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2006.08.055; PII: S0042-6822(06)00578-2; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ANTIBODIES; CELL MEMBRANES; GLYCOPROTEINS; MEMBRANE PROTEINS; VIRUSES

Citation Formats

Govero, Jennifer, Hall, Susan, and Heineman, Thomas C. Intracellular localization of varicella-zoster virus ORF39 protein and its functional relationship to glycoprotein K. United States: N. p., 2007. Web. doi:10.1016/j.virol.2006.08.055.
Govero, Jennifer, Hall, Susan, & Heineman, Thomas C. Intracellular localization of varicella-zoster virus ORF39 protein and its functional relationship to glycoprotein K. United States. doi:10.1016/j.virol.2006.08.055.
Govero, Jennifer, Hall, Susan, and Heineman, Thomas C. Tue . "Intracellular localization of varicella-zoster virus ORF39 protein and its functional relationship to glycoprotein K". United States. doi:10.1016/j.virol.2006.08.055.
@article{osti_20975214,
title = {Intracellular localization of varicella-zoster virus ORF39 protein and its functional relationship to glycoprotein K},
author = {Govero, Jennifer and Hall, Susan and Heineman, Thomas C.},
abstractNote = {Varicella-zoster virus (VZV) encodes two multiply inserted membrane proteins, open reading frame (ORF) 39 protein (ORF39p) and glycoprotein K (gK). The HSV-1 homologs of these proteins are believed to act in conjunction with each other during viral egress and cell-cell fusion, and they directly influence each other's intracellular trafficking. However, ORF39p and VZV gK have received very limited study largely due to difficulties in producing antibodies to these highly hydrophobic proteins. To overcome this obstacle, we introduced epitope tags into both ORF39p and gK and examined their intracellular distributions in transfected and infected cells. Our data demonstrate that both ORF39p and gK accumulate predominately in the ER of cultured cells when expressed in the absence of other VZV proteins or when coexpressed in isolation from other VZV proteins. Therefore, the transport of VZV ORF39p and gK does not exhibit the functional interdependence seen in their HSV-1 homologs. However, during infection, the primary distributions of ORF39p and gK shift from the ER to the Golgi, and they are also found in the plasma membrane indicating that their intracellular trafficking during infection depends on other VZV-encoded proteins. During infection, ORF39p and gK tightly colocalize with VZV envelope glycoproteins B, E and H; however, the coexpression of ORF39p or gK with other individual viral glycoproteins is insufficient to alter the transport of either ORF39p or gK.},
doi = {10.1016/j.virol.2006.08.055},
journal = {Virology},
number = 2,
volume = 358,
place = {United States},
year = {Tue Feb 20 00:00:00 EST 2007},
month = {Tue Feb 20 00:00:00 EST 2007}
}